The relationship between binding forces and the catalysis of organic chemical reactions is to be explored using a new model. The binding forces are used to move remote atoms along a reaction coordinate in such a manner that activation barriers for reactions are reduced. As such, these systems offer models for enzyme catalysis involving maximum binding to a transition state. Specific applications include catalysis of substitution reactions, acyl transfers and phosphate hydrolysis. In addition, binding-induced conformational changes are examined in molecules which permit interactions between remote sites. Binding and transport of ions with these molecules provides model systems for the allosteric effects of enzymology, especially those subunit systems such as hemoglobin which show positive cooperativity.